ArticleThe protein journal2014
Isolation, functional characterization and proteomic identification of CC2-PLA₂ from Cerastes cerastes venom: a basic platelet-aggregation-inhibiting factor.
Article in The protein journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 22 citations in OpenAlex.
- Structural, Biochemical Characterization and Molecular Mechanism of Cerastokunin: A New Kunitz-Type Peptide with Potential Inhibition of Thrombin, Factor Xa and Platelets.The protein journal · 2024Article
- Functional Characterization and Anti-Tumor Effect of a Novel Group II Secreted Phospholipase AMolecules (Basel, Switzerland) · 2023Article
- Therapeutic Outcome of Anti-inflammatory and Antioxidative Medicines on the Dermonecrotic Activity of Cerastes cerastes Venom.Inflammation · 2022Article
- Review
- Bioactive Molecules Derived from Snake Venoms with Therapeutic Potential for the Treatment of Thrombo-Cardiovascular Disorders Associated with COVID-19.The protein journal · 2021Review
- "Computational and Functional Characterization of a Hemorrhagic Metalloproteinase Purified from Cerastes cerastes Venom".The protein journal · 2021Article
- Experimental Lachesis muta rhombeata envenomation and effects of soursop (Annona muricata) as natural antivenom.The journal of venomous animals and toxins including tropical diseases · 2016Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Three-step chromatography and proteomic analysis have been used to purify and characterize a new basic phospholipase A₂ named CC2-PLA₂ from the venom of Cerastes cerastes. This phospholipase A₂ has been isolated to an extent of about 50-folds and its molecular weight was estimated at 13,534 Da. For CC2-PLA₂ identification and LC-MALDI-MS/MS analysis, the protein was reduced, alkylated and double hydrolyzed by lysine-C endopeptidase and trypsin. Tryptic fragments of LC-MS/MS analyzed CC2-PLA₂ showed sequence similarities with other snake venom PLA₂. This presents only 51 % (61/120 amino acid residues) sequence homology with the first PLA₂ (gi |129506|) previously purified from the same venom. The isolated CC2-PLA₂ displayed anti-aggregative effect on platelets and induced an inflammatory response characterized by leukocytosis in the peripheral blood. This inflammatory response is accompanied by a release of inflammatory mediators such as IL-6, eosinophil peroxidase and complement system. Obtained results indicate that CC2-PLA₂ induced a release of high level of pro-inflammatory (IL-6) cytokine and no effect on the level of anti-inflammatory cytokine (IL-10) in blood sera. Furthermore, eosinophil peroxidase activity and hemolytic complement effect increased in peripheral blood. Mononuclear and neutrophil cells were found predominant in the induced leucocytosis following CC2-PLA₂ administration into animals.
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